Structure of thymidylate kinase from Ehrlichia chaffeensis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1090-4. doi: 10.1107/S174430911101493X. Epub 2011 Aug 16.

Abstract

The enzyme thymidylate kinase phosphorylates the substrate thymidine 5'-phosphate (dTMP) to form thymidine 5'-diphosphate (dTDP), which is further phosphorylated to dTTP for incorporation into DNA. Ehrlichia chaffeensis is the etiologic agent of human monocytotropic erlichiosis (HME), a potentially life-threatening tick-borne infection. HME is endemic in the United States from the southern states up to the eastern seaboard. HME is transmitted to humans via the lone star tick Amblyomma americanum. Here, the 2.15 Å resolution crystal structure of thymidylate kinase from E. chaffeensis in the apo form is presented.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Crystallography, X-Ray
  • Ehrlichia chaffeensis / enzymology*
  • Humans
  • Models, Molecular
  • Nucleoside-Phosphate Kinase / chemistry*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Structural Homology, Protein

Substances

  • Nucleoside-Phosphate Kinase
  • dTMP kinase

Associated data

  • PDB/3LD9